The enzyme, which was characterized from dormant seeds of the plant Cajanus cajan (pigeon pea), has been shown to remove the terminal non-reducing beta-L-arabinopyranoside residue from the artificial substrate p-nitrophenyl-beta-L-arabinopyranose [1]. In the presence of methanol the enzyme demonstrates transglycosylase activity, transferring the arabinose moiety to methanol while retaining the anomeric configuration, generating 1-O-methyl-beta-L-arabinopyranose [2].

comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major